Structural highlights
Function
[HIP_THETI] Specific class of high-redox-potential 4Fe-4S ferredoxins. Functions in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Crystals of the high-potential iron-sulfur protein (HiPIP) from Thermochromatium tepidum diffract X-rays to 0.80 A using synchrotron radiation at 100 K. The crystal structure of this HiPIP was refined at this ultrahigh resolution with anisotropic temperature factors for all atoms to conventional crystallographic R factors of 0.092 and 0.101 for F(o) > 4sigma(F(o)) and all reflections, respectively. The present structure provides a more precise picture than the previous 1.5 A structure and allows location of the positions of most H atoms. The structure revealed a partly hydrophobic cavity near the main hydrophobic area and a much larger inter-cluster approach distance (23.454 A, the c constant of the unit cell) in the crystal packing than other types of HiPIPs. The structural features involved in the electron-transfer reaction of HiPIP are discussed.
Ultrahigh-resolution structure of high-potential iron-sulfur protein from Thermochromatium tepidum.,Liu L, Nogi T, Kobayashi M, Nozawa T, Miki K Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1085-91. Epub 2002, Jun 20. PMID:12077426[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu L, Nogi T, Kobayashi M, Nozawa T, Miki K. Ultrahigh-resolution structure of high-potential iron-sulfur protein from Thermochromatium tepidum. Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1085-91. Epub 2002, Jun 20. PMID:12077426
